Abstract
The irreversible inhibition of 8-amino-7-oxononanoate synthase by trifluoroalanine involves decarboxylative defluorination of the inhibitor-PLP aldimine followed by attack of the conjugated imine by the amino group of the active site lysine to afford a covalently bound difluorinated intermediate which can subsequently undergo further HF losses and hydrolysis to afford a 2-(pyridoximine phosphate) acetoyl protein adduct.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acyltransferases / antagonists & inhibitors
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Acyltransferases / chemistry*
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Acyltransferases / metabolism*
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Alanine / analogs & derivatives*
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Alanine / metabolism*
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Binding Sites
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Catalysis
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Hydrolysis
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Ligases / antagonists & inhibitors*
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Lysine / chemistry
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Models, Molecular
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Protein Conformation
Substances
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Acyltransferases
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8-amino-7-oxononanoate synthase
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Ligases
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Lysine
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Alanine